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PMID: 6326142 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Mechanism of the concerted action of recA protein and helix-destabilizing proteins in homologous recombination.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 81 ·No. 9 ·1984-05-00 ·Pages 2757-61

Muniyappa K, Shaner SL, Tsang SS, Radding CM

Abstract

Secondary structure in single-stranded DNA impedes the presynaptic association of recA protein and consequently blocks the formation of joint molecules as evidenced by effects of temperature, nucleotide sequence, and ionic conditions. Escherichia coli single-strand-binding protein eliminates sequence-specific "cold spots" by removing folds even from sites of strong secondary structure. Thus, destabilization of secondary structure in single-stranded DNA is critical for the action of recA protein, whereas specific interactions directly between helix-destabilizing proteins and recA protein are unimportant.

MeSH Terms
Base Sequence DNA Helicases/genetics DNA, Single-Stranded/genetics DNA-Binding Proteins/genetics Magnesium/physiology Nucleic Acid Conformation Protein Binding Rec A Recombinases/genetics Recombination, Genetic Temperature Viral Proteins
Chemicals
DNA, Single-Stranded DNA-Binding Proteins Viral Proteins gp32 protein, Enterobacteria phage T4 helix-destabilizing proteins Rec A Recombinases DNA Helicases Magnesium
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Muniyappa K
Shaner S L
Tsang S S
Radding C M
References (33)
33 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.81.9.2757
Published
1984-05-00
Pages
2757-61
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC345149
Subset
IM
Grants
NIGMS NIH HHS · GM 30488 · United States
External Links
PubMed source DOI: 10.1073/pnas.81.9.2757 PMC Full Text View journal details
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